Chlorine in PDB 6v72: Crystal Structure of Metallo Beta Lactamase From Erythrobacter Litoralis

The structure of Crystal Structure of Metallo Beta Lactamase From Erythrobacter Litoralis, PDB code: 6v72 was solved by N.Maltseva, Y.Kim, S.Clancy, M.Endres, R.Mulligan, A.Joachimiak, Center Forstructural Genomics Of Infectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.06 / 1.50
Space group	P 3 2 1
Cell size a, b, c (Å), α, β, γ (°)	96.985, 96.985, 45.186, 90.00, 90.00, 120.00
R / Rfree (%)	14.9 / 18.3

The structure of Crystal Structure of Metallo Beta Lactamase From Erythrobacter Litoralis also contains other interesting chemical elements:

Calcium

(Ca)

3 atoms

The binding sites of Chlorine atom in the Crystal Structure of Metallo Beta Lactamase From Erythrobacter Litoralis (pdb code 6v72). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Crystal Structure of Metallo Beta Lactamase From Erythrobacter Litoralis, PDB code: 6v72:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Crystal Structure of Metallo Beta Lactamase From Erythrobacter Litoralis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Metallo Beta Lactamase From Erythrobacter Litoralis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl304 b:27.1 occ:1.00 OG1 A:THR182 3.1 21.2 1.0 O A:HOH441 3.1 37.8 1.0 O A:HOH408 3.1 25.8 1.0 N A:ALA113 3.2 22.0 1.0 OG A:SER137 3.3 28.8 0.4 CA A:HIS112 3.7 19.1 1.0 CB A:THR182 3.8 18.4 1.0 C A:ASP184 3.9 14.9 1.0 CB A:ASP184 3.9 20.0 1.0 C A:HIS112 3.9 21.5 1.0 CB A:SER137 4.0 31.4 0.6 CB A:ALA113 4.0 26.4 1.0 N A:ASN185 4.1 12.6 1.0 CB A:HIS112 4.1 24.3 1.0 O A:ASP184 4.1 17.7 1.0 CB A:SER137 4.2 28.9 0.4 CA A:ASP184 4.2 17.5 1.0 CA A:ALA113 4.2 25.9 1.0 N A:ASP184 4.2 15.5 1.0 CG2 A:THR182 4.4 21.9 1.0 CA A:SER137 4.4 28.2 0.6 CA A:SER137 4.5 27.3 0.4 CA A:ASN185 4.6 12.0 1.0 OD2 A:ASP184 4.8 28.6 1.0 CG A:ASP184 4.9 24.1 1.0 N A:HIS112 4.9 14.0 1.0 O A:THR111 5.0 15.3 1.0

Chlorine binding site 2 out of 4 in the Crystal Structure of Metallo Beta Lactamase From Erythrobacter Litoralis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Metallo Beta Lactamase From Erythrobacter Litoralis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl305 b:15.7 occ:0.33 N A:ALA157 3.1 14.4 1.0 CB A:ASP156 3.5 14.5 1.0 CA A:ASP156 3.6 13.4 1.0 CB A:ALA157 3.8 18.8 1.0 C A:ASP156 3.8 12.5 1.0 CA A:ALA157 4.1 16.5 1.0 CG A:ASP156 4.6 15.6 1.0 N A:ASP156 4.9 12.5 1.0

Chlorine binding site 3 out of 4 in the Crystal Structure of Metallo Beta Lactamase From Erythrobacter Litoralis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Metallo Beta Lactamase From Erythrobacter Litoralis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl306 b:23.6 occ:1.00 O A:HOH462 3.1 23.5 1.0 N A:ASP234 3.3 20.4 1.0 C A:PHE232 3.4 17.3 1.0 N A:ALA235 3.4 19.5 1.0 CA A:PHE232 3.4 14.9 1.0 N A:PRO233 3.6 16.5 1.0 CD A:PRO233 3.7 18.2 1.0 CB A:PHE232 3.8 16.1 1.0 O A:PHE232 3.8 17.1 1.0 CA A:ASP234 3.9 21.8 1.0 CB A:ASP234 4.0 24.2 1.0 O A:HOH435 4.0 28.1 1.0 CB A:ALA235 4.0 18.0 1.0 C A:ASP234 4.0 22.7 1.0 CA A:ALA235 4.2 19.1 1.0 CB A:PRO191 4.3 19.2 1.0 C A:PRO233 4.3 19.1 1.0 CA A:PRO191 4.4 19.3 1.0 CD1 A:PHE232 4.4 16.2 1.0 CA A:PRO233 4.5 16.4 1.0 OD2 A:ASP234 4.6 32.3 1.0 CG A:PRO233 4.6 19.2 1.0 CG A:PHE232 4.7 15.1 1.0 CG A:ASP234 4.7 28.8 1.0 N A:PHE232 4.8 14.9 1.0 CG A:PRO191 4.8 19.8 1.0 O A:ALA231 4.9 16.2 1.0 O A:PRO191 4.9 23.9 1.0

Chlorine binding site 4 out of 4 in the Crystal Structure of Metallo Beta Lactamase From Erythrobacter Litoralis


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of Metallo Beta Lactamase From Erythrobacter Litoralis within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl311 b:37.2 occ:1.00 O A:HOH472 3.2 28.0 1.0 N A:LEU210 3.2 18.3 1.0 O A:HOH502 3.5 37.0 1.0 CA A:ASN209 3.7 20.1 1.0 CB A:ASN209 3.8 22.9 1.0 CB A:LEU210 3.9 15.6 1.0 C A:ASN209 4.0 18.7 1.0 CG A:LEU210 4.0 15.3 1.0 CA A:LEU210 4.1 16.8 1.0 CD1 A:LEU213 4.2 22.4 1.0 CD2 A:LEU261 4.3 21.8 1.0 CD1 A:LEU210 4.4 15.1 1.0 O A:HOH560 4.4 39.4 1.0 C A:LEU210 4.9 18.8 1.0

N.Maltseva, Y.Kim, S.Clancy, M.Endres, R.Mulligan, A.Joachimiak, Center For Structural Genomics Of Infectious Diseases(Csgid). Crystal Structure of Metallo Beta Lactamase From Erythrobacter Litoralis To Be Published.